Monoclonal Antibodies to Enzymes

  • Harry Harris


The application of immunological methods to problems in enzymology has a long history and a very extensive literature. For the most part, this deals with studies using antisera raised against purified enzymes in animals of species other than those from which the enzymes were derived. The use of monoclonal antibodies is, of course, much more recent. Such antibodies have so far only been produced against a modest number of enzymes, though new reports are appearing at an increasing pace and there is little doubt that before long, such antibodies will become the reagents of choice for a wide variety of studies in enzyme immunochemistry. The analytic power of monoclonal antibodies in enzymology largely derives from the fact that each antibody is directed to an antigenic determinant that represents only a small region on the surface of the enzyme protein. Consequently, many antibodies with distinctive specificities can in principle be raised against a single enzyme. This contrasts with antisera, which contain a complex mixture of antibodies directed to different determinants on the enzyme surface and occurring in unknown proportions. The other important advantage is that monoclonal antibodies are single immunoglobulin species, which can, in principle, be produced in unlimited quantities by continued culture of the hybridoma cells that secrete them, whereas the antibody composition of antisera will vary in any particular animal during the course of immunization and will vary from animal to animal immunized with the same antigen.


Monoclonal Antibody Guanylate Cyclase Antigenic Determinant Binding Ratio Sialic Acid Residue 
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Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Harry Harris
    • 1
  1. 1.Department of Human GeneticsUniversity of Pennsylvania School of MedicinePhiladelphiaUSA

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